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1K6C

LACK OF SYNERGY FOR INHIBITORS TARGETING A MULTI-DRUG RESISTANT HIV-1 PROTEASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
B0004190molecular_functionaspartic-type endopeptidase activity
B0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 501
ChainResidue
APRO1
BHIS69
BLYS70
BHOH938

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT B 502
ChainResidue
APRO39
AGLY40
BMET36
BASN37

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 503
ChainResidue
BARG14
BGLY16
BGLY17
BHOH963
AGLY17

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT B 504
ChainResidue
BTHR74
BASN88

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT B 506
ChainResidue
BPRO1
BARG57
BHIS69
BHOH929
BHOH940
BHOH959

site_idAC6
Number of Residues19
DetailsBINDING SITE FOR RESIDUE MK1 B 902
ChainResidue
AARG8
AASP25
AGLY27
AILE47
AGLY48
AGLY49
AHOH513
BARG8
BASP25
BGLY27
BALA28
BASP29
BASP30
BVAL32
BGLY48
BILE50
BPRO81
BHOH905
BHOH927

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL
ChainResidueDetails
AALA22-LEU33

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Cleavage; by viral protease => ECO:0000250
ChainResidueDetails
ALEU76
BLEU76

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by host => ECO:0000250
ChainResidueDetails
ALEU76
BLEU76

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
ATHR26
BASP25
BTHR26

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a30
ChainResidueDetails
AASP25
BASP25

223166

PDB entries from 2024-07-31

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